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AB94288

Estrogen Sulfotransferase overexpression 293T lysate (whole cell)

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Estrogen Sulfotransferase overexpression 293T lysate (whole cell) suitable for WB. View our extensive range of validated lysates from normal and diseased human, mouse and rat tissue.

View Alternative Names

Estrogen sulfotransferase, ST1E1_HUMAN, STE, SULT1E1, Sulfotransferase, Sulfotransferase 1E1, Sulfotransferase estrogen preferring, Sulfotransferase family 1E member 1, estrogen-preferring, estrone sulfotransferase

2 Images
Western blot - Estrogen Sulfotransferase overexpression 293T lysate (whole cell) (AB94288)
  • WB

Unknown

Western blot - Estrogen Sulfotransferase overexpression 293T lysate (whole cell) (AB94288)

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SDS-PAGE - Estrogen Sulfotransferase overexpression 293T lysate (whole cell) (AB94288)
  • SDS-PAGE

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SDS-PAGE - Estrogen Sulfotransferase overexpression 293T lysate (whole cell) (AB94288)

ab94288 at 15µg/lane on an SDS-PAGE gel.

Key facts

Species or organism

Human

Form

Liquid

form

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "WB": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Product details

ab94288 is a 293T cell transfected lysate in which Human Estrogen Sulfotransferase has been transiently over-expressed using a pCMV-Estrogen Sulfotransferase plasmid. The lysate is provided in 1X Sample Buffer.

Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-20°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Estrogen Sulfotransferase also known as SULT1E1 is an enzyme that catalyzes the sulfonation of estrogens converting them into inactive sulfated estrogens. This enzyme mainly transfers a sulfate group from the universal donor 3'-phosphoadenosine-5'-phosphosulfate (PAPS) to estrone and estradiol. Estrogen Sulfotransferase has a molecular mass of approximately 34 kDa. It is expressed primarily in the liver intestine endometrium and other tissues that need to regulate estrogen activity.
Biological function summary

Estrogen Sulfotransferase impacts estrogen regulation helping to maintain hormone balance and modulate receptor binding affinity. It is not part of any known enzyme complexes but interacts with substrates and cofactors to perform its function. The enzyme modulates the biological availability of estrogen impacting growth reproductive function and lipid metabolism. By sulfating estrogens the enzyme prevents their interaction with estrogen receptors effectively inactivating them and controlling their bioavailability.

Pathways

The enzymatic activity of Estrogen Sulfotransferase contributes significantly to estrogen metabolism and hormonal regulation pathways. It is particularly active in the steroid hormone biosynthesis pathway working alongside the cytochrome P450 family of enzymes. In these pathways Estrogen Sulfotransferase indirectly influences metabolic processes through its modulation of active estrogens. By limiting the concentration of free estrogens it affects downstream signaling pathways that influence cellular processes like cell growth and differentiation.

Dysregulation of Estrogen Sulfotransferase activity is associated with hormone-dependent cancers such as breast and endometrial cancer due to its role in managing estrogen levels. The enzyme's function becomes critical when overactive estrogen signaling contributes to disease progression. The relationship with Estrogen Receptor alpha (ERα) is pivotal as altered sulfotransferase activity can influence receptor-mediated signaling. Additionally variations or mutations affecting Estrogen Sulfotransferase's regulation of estrogen metabolism can link to conditions like polycystic ovary syndrome (PCOS) impacting hormonal and metabolic balances.

Cell culture

Product protocols

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